2000
Identification and Characterization of βV Spectrin, a Mammalian Ortholog of Drosophila βHSpectrin* 210
Stabach P, Morrow J. Identification and Characterization of βV Spectrin, a Mammalian Ortholog of Drosophila βHSpectrin* 210. Journal Of Biological Chemistry 2000, 275: 21385-21395. PMID: 10764729, DOI: 10.1074/jbc.c000159200.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceCaenorhabditis elegansCloning, MolecularConsensus SequenceDNA, ComplementaryDrosophilaDrosophila ProteinsExonsGene LibraryHumansIntronsMammalsMolecular Sequence DataMolecular WeightOrgan SpecificityPhylogenyRatsRecombinant ProteinsRepetitive Sequences, Amino AcidRetinaSequence AlignmentSequence Homology, Amino AcidSpectrinTumor Cells, CulturedViral ProteinsConceptsDrosophila orthologMammalian orthologsSpectrin repeatsPleckstrin homology domainComplete cDNA sequenceActin-binding domainSelf-association domainAmino acids 85Amino acid sequenceBeta-spectrin geneHuman retina cDNA libraryRetina cDNA libraryFly counterpartMammalian spectrinsCaenorhabditis elegansHomology domainEpithelial cell populationsSH3 domainApical domainCDNA sequenceCDNA libraryOrthologsPolarized epitheliumBeta spectrinAcid sequence
1998
A widely expressed βIII spectrin associated with Golgi and cytoplasmic vesicles
Stankewich M, Tse W, Peters L, Ch’ng Y, John K, Stabach P, Devarajan P, Morrow J, Lux S. A widely expressed βIII spectrin associated with Golgi and cytoplasmic vesicles. Proceedings Of The National Academy Of Sciences Of The United States Of America 1998, 95: 14158-14163. PMID: 9826670, PMCID: PMC24343, DOI: 10.1073/pnas.95.24.14158.Peer-Reviewed Original ResearchConceptsBetaIII spectrinGene mapsMembrane skeletonEndoplasmic reticulum marker calnexinPlasma membrane skeletonPleckstrin homology domainTrans-Golgi networkHuman brain cDNASyntenic regionsGene familyProtein 4.1Membrane associationCompartment markersImportant structural componentDa proteinSelf-association siteGolgi membranesHomology searchCDNA endsRapid amplificationUnidentified isoformChromosome 19Liver Golgi membranesGenBank databaseVesicle markersADP ribosylation factor regulates spectrin binding to the Golgi complex
Godi A, Santone I, Pertile P, Devarajan P, Stabach P, Morrow J, Di Tullio G, Polishchuk R, Petrucci T, Luini A, De Matteis M. ADP ribosylation factor regulates spectrin binding to the Golgi complex. Proceedings Of The National Academy Of Sciences Of The United States Of America 1998, 95: 8607-8612. PMID: 9671725, PMCID: PMC21123, DOI: 10.1073/pnas.95.15.8607.Peer-Reviewed Original ResearchConceptsADP-ribosylation factorGolgi complexRibosylation factorG proteinsVesicular stomatitis virus G proteinPleckstrin homology domainSmall G proteinsPH domain interactionBinding of spectrinVirus G proteinGolgi spectrinHomology domainPH domainCoat proteinDocking siteDomain interactionsGolgiEndoplasmic reticulumPtdInsP2 levelsDomain IPhospholipase DSpectrinGolgi fractionsProteinPtdInsP2Utilization of an 86bp exon generates a novel adducin isoform (β4) lacking the MARCKS homology domain1The first two authors contributed equally to this work.1
Sinard J, Stewart G, Stabach P, Argent A, Gilligan D, Morrow J. Utilization of an 86bp exon generates a novel adducin isoform (β4) lacking the MARCKS homology domain1The first two authors contributed equally to this work.1. Biochimica Et Biophysica Acta 1998, 1396: 57-66. PMID: 9524222, DOI: 10.1016/s0167-4781(97)00167-x.Peer-Reviewed Original ResearchMeSH KeywordsAlternative SplicingAmino Acid SequenceBase SequenceCalmodulin-Binding ProteinsCloning, MolecularExonsHumansIntracellular Signaling Peptides and ProteinsIsomerismMembrane ProteinsMolecular Sequence DataMyristoylated Alanine-Rich C Kinase SubstrateOrgan SpecificityPolymerase Chain ReactionProtein Structure, TertiaryProteinsSequence Homology, Amino AcidSequence Homology, Nucleic AcidTranscription, GeneticConceptsNovel amino acidAmino acidsBeta-adducinNew isoformHuman bone marrow cDNA libraryBone marrow cDNA libraryDifferent reading framesCalcium/calmodulinLysine-rich sequenceNT-2 cellsProtein kinase CGenomic clonesGenomic mapNew amino acidsAlternate exonsActin crossCDNA libraryReading frameSplice consensus sequenceNew exonsNovel isoformConsensus sequenceStop codonKinase CExons
1997
Na,K-ATPase transport from endoplasmic reticulum to Golgi requires the Golgi spectrin–ankyrin G119 skeleton in Madin Darby canine kidney cells
Devarajan P, Stabach P, De Matteis M, Morrow J. Na,K-ATPase transport from endoplasmic reticulum to Golgi requires the Golgi spectrin–ankyrin G119 skeleton in Madin Darby canine kidney cells. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 10711-10716. PMID: 9380700, PMCID: PMC23456, DOI: 10.1073/pnas.94.20.10711.Peer-Reviewed Original ResearchConceptsMembrane proteinsEndoplasmic reticulumSpectrin skeletonVesicular tubular clustersActin-binding domainSpecific membrane proteinsMadin-Darby canine kidney cellsK-ATPase transportCanine kidney cellsDynactin complexVesicle traffickingCargo proteinsGolgi spectrinTrafficking systemBeta-COPMembrane compartmentsTransport of alphaAdapter proteinCis-GolgiGolgi membranesGolgi stacksDocking complexBetaI spectrinGolgiBeta NASite-Directed Mutagenesis of αII Spectrin at Codon 1175 Modulates Its μ-Calpain Susceptibility †
Stabach P, Cianci C, Glantz S, Zhang Z, Morrow J. Site-Directed Mutagenesis of αII Spectrin at Codon 1175 Modulates Its μ-Calpain Susceptibility †. Biochemistry 1997, 36: 57-65. PMID: 8993318, DOI: 10.1021/bi962034i.Peer-Reviewed Original ResearchConceptsSite-directed mutagenesisAlpha II spectrinCalpain cleavage sitesCleavage siteII-spectrinHelix CRecombinant GST-fusion proteinsBona fide proteinGST fusion proteinTriple-helical motifsStrict substrate specificityFamily of Ca2Protein kinase CDynamic molecular modelingStructural repeatsProminent substrateDifferent amino acidsSubstrate specificityIntracellular proteolysisPenultimate residueCysteine proteasesKinase CMost proteasesSteroid receptor activationSpectrin